Proton transfer is the essence of acid-base catalysis and hence fundamental to the action of most enzymes. Bio-organic chemists have, therefore, directed an enormous amount of effort toward the attainment of a complete description of proton transfer reactions in water. This work has, however largely neglected the powerful dynamic NMR method as a tool for studying proton transfers. Considering that proton transfer is an important and often rate determining aspect of enzyme "model" systems, the scarcity of pmr data in bio-organic chemistry constitutes a sizeable void. In view of this situation, are applying the dynamic NMR method to biologically interesting proton transfers as well as to other fast reactions. This work will include studies of amide proton exchange in both aqueous and non-aqueous solvents; intramolecularly and bifunctionally catalyzed proton transfers; proton transfers on micelle surfaces; the mechanism of proton exchange of hydrogen bonded alcohols; molecular motion within charge-transfer complexes. We are also undertaking an investigation of proton exchange and inversion reactions of endo- and exo-2-dimethylaminonorbornane, the results of which have a bearing on the orbital steering theory for enzyme action. BIBLIOGRAPHIC REFERENCES: F.M. Menger, H.K. Rhee, and J.U. Rhee, J. Amer. Chem. Soc., 98, 792 (1976). "Proton Exchange in Benzyl Alcohols. Acid, Base, Intramolecular, and Bifunctional Catalyses." F.M. Menger and K.S. Venkatasubban, J. Org. Chem., 41, 1868 (1976). "Proton Inventory Study of a Water-Catalyzed Hydrolysis."